Interaction of bovine heart pyruvate kinase with phospholipids.

A Dabrowska, G Terlecki, E Czapińska, J Gutowicz

Other Biochimica et biophysica acta 1995 7 trích dẫn

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Study Design

Loại nghiên cứu: Other
Đối tượng nghiên cứu: general population

Can thiệp: Interaction of bovine heart pyruvate kinase with phospholipids. None
Đối chứng: None
Kết quả chính: lipid levels
Xu hướng hiệu quả: Mixed
Nguy cơ sai lệch: Moderate

Abstract

The interaction between bovine heart pyruvate kinase and liposomes was investigated for various phospholipids as function of pH, and salt concentration using steady-state kinetics and ultracentrifugation. Liposomes made from erythrocyte total lipid fraction and individual phospholipids were used. Pyruvate kinase specific activity increases upon the interaction with the phospholipids. The activation is specifically sensitive to presence of phosphatidylserine in liposomes. L-serine, and phospho-L-serine which are main components of phosphatidylserine head group show also some activation effect. Efficient adsorption of pyruvate kinase to phosphatidylserine liposomes occurs in the pH range 6.0-8.0 and at low ionic strength. Interaction with phosphatidylserine liposomes results in the change of Vmax and Km values for phospho enol pyruvate without marked effect on Km value for ADP, and Hill coefficients for both substrates. The interaction does not seem to influence the cooperativity between binding sites.

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Interaction of bovine heart pyruvate kinase with phospholipids.

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Study Design

Abstract

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